Evolution of Protein Quaternary Structure in Response to Selective Pressure for Increased Thermostability
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- 作者：Nicholas J. Fraser1 ; Jian-Wei Liu2 ; Peter D. Mabbitt1 ; Galen J. Correy1 ; Chris W. Coppin2 ; Mathilde Lethier3 ; Matthew A. Perugini4 ; James M. Murphy5 ; 6 ; John G. Oakeshott2 ; Martin Weik3 ; Colin J. Jackson1 ; cjackson@rsc.anu.edu.au" class="auth_mail" title="E-mail the corresponding author
- 关键词：oligomerization ; directed evolution ; thermostability ; carboxylesterase ; interface
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：5 June 2016
- 年：2016
- 卷：428
- 期：11
- 页码：2359-2371
- 全文大小：1255 K
文摘
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The extent to which natural selection promotes oligomerization is unknown.
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Directed evolution and selection for stability resulted in increased oligomerization.
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A tradeoff between thermostability and enzymatic activity was observed.
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Oligomerization may be an evolutionary strategy for protein stabilization.